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1.
Reproduction ; 167(5)2024 May 01.
Artículo en Inglés | MEDLINE | ID: mdl-38471304

RESUMEN

In brief: HSP90AA1 is a ubiquitous molecular chaperone that can resist cellular stress, such as oxidative stress and apoptosis, and mediate the efficacy and protein folding of normal cells during heat stress, as well as many other functions. This study further reveals the role of HSP90AA1 in bovine oocyte maturation and early embryonic development. Abstract: HSP90AA1, a highly abundant and ubiquitous molecular chaperone, plays important roles in various cellular processes including cell cycle control, cell survival, and hormone signaling pathways. In this study, we investigated the functions of HSP90AA1 in bovine oocyte and early embryo development. We found that HSP90AA1 was expressed at all stages of development, but was mainly located in the cytoplasm, with a small amount distributed in the nucleus. We then evaluated the effect of HSP90AA1 on the in vitro maturation of bovine oocytes using tanespimycin (17-AAG), a highly selective inhibitor of HSP90AA1. The results showed that inhibition of HSP90AA1 decreased nuclear and cytoplasmic maturation of oocytes, disrupted spindle assembly and chromosome distribution, significantly increased acetylation levels of α-tubulin in oocytes and affected epigenetic modifications (H3K27me3 and H3K27ac). In addition, H3K9me3 was increased at various stages during early embryo development. Finally, the impact of HSP90AA1 on early embryo development was explored. The results showed that inhibition of HSP90AA1 reduced the cleavage and blastocyst formation rates, while increasing the fragmentation rate and decreasing blastocyst quality. In conclusion, HSP90AA1 plays a crucial role in bovine oocyte maturation as well as early embryo development.


Asunto(s)
Proteínas HSP90 de Choque Térmico , Oocitos , Oogénesis , Animales , Bovinos , Blastocisto/metabolismo , Desarrollo Embrionario , Técnicas de Maduración In Vitro de los Oocitos/métodos , Chaperonas Moleculares/metabolismo , Chaperonas Moleculares/farmacología , Oocitos/metabolismo , Oogénesis/genética , Proteínas HSP90 de Choque Térmico/antagonistas & inhibidores , Proteínas HSP90 de Choque Térmico/metabolismo
2.
Dev Comp Immunol ; 100: 103413, 2019 11.
Artículo en Inglés | MEDLINE | ID: mdl-31200007

RESUMEN

The objective of this study is to explore the immune response of the shrimp Penaeus vannamei to low temperature and air exposure during the mimic waterless transportation. Shrimp were cold shocked at 13 °C for 3 min, then exposed to air at 15 °C for 12 h, and finally revived in water at 25 °C. Hemocyte structure remained intact with only slight distortions of some organelles and nuclear membrane under the stress. Phenoloxidase (PO), lysozyme (Lys) and gamma-glutamyl transferase (GGT) activities, glutamine (Gln) content and relative mRNA expressions of prophenoloxidase (proPO), ß-1,3-glucan binding protein (LGBP), ferrin (Fer) and glucose regulated protein 78 (GRP 78) increased and reached peak levels after 3 h-9 h of air exposure, and then decreased to relatively stable levels in the prolonged period of air exposure. The total hemocyte count (THC) and gene expressions of proPO, Fer and LGBP at the end of waterless storage were significantly lower (p < 0.05) than those in fresh shrimp while no significant difference (p ≥ 0.05) was found between revived and fresh shrimp in PO, Lys, GGT activities, Gln content and gene expression level of GRP 78. Of all the hemocytes, the percentage of semi granular cells (SGC) and granular cells (GC) significantly decreased after 6-9 h of storage, while hyaline cells (HC) dramatically increased after 9 h of storage to compensate the loss of SGC and GC. Results suggested that the low temperature and air exposure caused significant immunological response to the shrimp, but the damages to the immune system were partly reparable.


Asunto(s)
Proteínas de Artrópodos/metabolismo , Regulación de la Expresión Génica/inmunología , Inmunidad/fisiología , Penaeidae/fisiología , Estrés Fisiológico/inmunología , Aire , Animales , Acuicultura , Frío/efectos adversos , Hemocitos/inmunología
3.
J Sci Food Agric ; 98(6): 2223-2230, 2018 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-28963774

RESUMEN

BACKGROUND: Rapid wound healing would be critical for successful long-term storage of fruits and vegetables. However, there was no direct evidence for the requirement and efficiency of oxygen in the fruit wound-healing process. This study was conducted to investigate the role of oxygen in wound-induced suberization by analyzing melanin, suberin polyphenolics (SPPs) and related enzymes in half-cut kiwifruits exposed to 100%, 50%, 21% and 0% oxygen. RESULTS: By 3 days after wounding, the wound surface of kiwifruit in high (50 and 100%) oxygen appeared as a continuous layer of melanin and SPPs underneath, which effectively prevent excessive water vapor loss from the fruit halves. In contrast, melanin and SPPs deposition in the wound surface in 0% oxygen was significantly reduced, with high water vapor loss. Rapid decrease of soluble phenolic acids (caffeic, p-coumaric, ferulic acids) was coupled with the increase of bound ferulic acid (coniferyl diacetate) especially in high oxygen by 9 days after wounding. Meanwhile, high oxygen enhanced peroxidase, catalase, phenylalanine ammonia-lyase, and polyphenol oxidase activities. CONCLUSION: Oxygen is required for wound-induced melanin and SPPs formation, and high oxygen is effective in promoting wound suberization in postharvest kiwifruit. © 2017 Society of Chemical Industry.


Asunto(s)
Actinidia/química , Lípidos/análisis , Oxígeno/análisis , Polifenoles/análisis , Actinidia/enzimología , Actinidia/metabolismo , Almacenamiento de Alimentos , Frutas/química , Frutas/enzimología , Frutas/metabolismo , Lípidos/biosíntesis , Melaninas/análisis , Melaninas/metabolismo , Oxidorreductasas/análisis , Oxidorreductasas/metabolismo , Oxígeno/metabolismo , Peroxidasa/análisis , Peroxidasa/metabolismo , Proteínas de Plantas/análisis , Proteínas de Plantas/metabolismo , Polifenoles/metabolismo
4.
Fish Shellfish Immunol ; 72: 564-571, 2018 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-29133253

RESUMEN

Low temperature and air exposure were the key attributes for waterless transportation of fish and shrimp. In order to investigate the oxidative stress and antioxidant responses of the live shrimp Litopenaeus vannamei in the mimic waterless transportation, live shrimp were cooled at 13 °C for 3 min, stored in oxygen at 15 °C for 12 h, and then revived in water at 25 °C. The survival rate of shrimp under this waterless transportation system was over 86.67%. The ultrastructure of hepatopancreas cells were observed while activities of superoxide dismutase (SOD), peroxidase (POD), catalase (CAT), glutathione peroxidase (GSH-Px), antisuperoxide anion free radicals (ASAFR), total antioxidant capacity (TAOC), reactive oxygen species (ROS) production, content of malondialdehyde (MDA) and relative mRNA expressions of CAT and GSH-Px in the hemolymph and hepatopancreas were determined. Slight distortions of some organelles in hepatopancreas cells was reversible upon the shrimp revived from the cold shock. The activities of SOD, POD, CAT, GSH-Px, TAOC, ROS production and relative mRNA expressions of CAT and GSH-Px increased following the cold shock and reached peak levels after 3 or 6 h of storage, and then decreased gradually. There was no significant difference between the fresh and the revived shrimp in SOD, POD, GSH-Px, TAOC, ROS, MDA and relative mRNA expressions of CAT and GSH-Px. The oxidative stress and antioxidant responses were tissue-specific because hepatopancreas seemed to have a greater ability to defend against organelle damage and was more sensitive to stress than hemolymph based on the results of SOD activity, MDA content and GSH-Px mRNA expression. These results revealed that low temperature and air exposure caused significant oxidative and antioxidant responses, but did not lead to irreversible damages in this waterless system.


Asunto(s)
Aire , Antioxidantes , Acuicultura/métodos , Frío/efectos adversos , Estrés Oxidativo , Penaeidae/fisiología , Animales , Hepatopáncreas/ultraestructura , Microscopía Electrónica de Transmisión , Penaeidae/enzimología , Penaeidae/ultraestructura , Transportes
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